Crystal structure of TFIID TATA-box binding protein

Dimitar B. Nikolov, Shu Hong Hu, Judith Lin, Alexander Gasch, Alexander Hoffmann, Masami Horikoshi, Nam Hai Chua, Robert G. Roeder, Stephen Burley

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Abstract

The structure of a central component of the eukaryotic transcriptional apparatus, a TATA-box binding protein (TBP or TFIIDτ) from Arabidopsis thaliana, has been determined by X-ray crystallography at 2.6 Å resolution. This highly symmetric α/β structure contains a new DMA-binding fold, resembling a molecular 'saddle' that sits astride the DMA. The DNA-binding surface is a curved, antiparallel β-sheet. When bound to DMA, the convex surface of the saddle would be presented for interaction with other transcription initiation factors and regulatory proteins.

Original languageEnglish (US)
Pages (from-to)40-46
Number of pages7
JournalNature
Volume360
Issue number6399
DOIs
StatePublished - Jan 1 1992
Externally publishedYes

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All Science Journal Classification (ASJC) codes

  • General

Cite this

Nikolov, D. B., Hu, S. H., Lin, J., Gasch, A., Hoffmann, A., Horikoshi, M., Chua, N. H., Roeder, R. G., & Burley, S. (1992). Crystal structure of TFIID TATA-box binding protein. Nature, 360(6399), 40-46. https://doi.org/10.1038/360040a0